Next Article in Journal
Analysis of Public Datasets for Wearable Fall Detection Systems
Next Article in Special Issue
Current Status of HbA1c Biosensors
Previous Article in Journal
Experimental Demonstration of Long-Range Underwater Acoustic Communication Using a Vertical Sensor Array
Previous Article in Special Issue
RAGE Plays a Role in LPS-Induced NF-κB Activation and Endothelial Hyperpermeability
Article Menu
Issue 7 (July) cover image

Export Article

Open AccessArticle
Sensors 2017, 17(7), 1515; doi:10.3390/s17071515

Exploitation of SPR to Investigate the Importance of Glycan Chains in the Interaction between Lactoferrin and Bacteria

1
Biosciences Department, Teagasc Food Research Centre, Moorepark, Fermoy, P61C996 Co. Cork, Ireland
2
Glycoscience Group, National Centre for Biomedical Engineering Science, National University of Ireland Galway, H91TK33, Galway, Ireland
*
Author to whom correspondence should be addressed.
Received: 15 May 2017 / Revised: 21 June 2017 / Accepted: 22 June 2017 / Published: 27 June 2017
(This article belongs to the Special Issue Sensors for Glycoproteins and Glycated Proteins)
View Full-Text   |   Download PDF [531 KB, uploaded 27 June 2017]   |  

Abstract

Bovine lactoferrin (LF) has been shown to prevent adhesion to and invasion of mammalian cell lines by pathogenic bacteria, with evidence for direct bacterial binding by the milk glycoprotein. However, the glycosylation pattern of LF changes over the lactation cycle. In this study, we aim to investigate the effect that this variation has on the milk glycoprotein’s ability to interact with pathogens. Surface plasmon resonance technology was employed to compare the binding of LF from colostrum (early lactation) and mature milk (late lactation) to a panel of pathogenic bacteria (Staphylococcus aureus, Escherichia coli, Cronobacter sakazakii, Streptococcus pneumoniae, Pseudomonas aeruginosa, Listeria monocytogenes and Salmonella typhimurium). Novel interactions with LF were identified for C. sakazakii, S. pneumoniae and P. aeruginosa with the highest binding ability observed for mature milk LF in all cases, with the exception of S. typhimurium. The difference in bacterial binding observed may be as a result of the varying glycosylation profiles. This work demonstrates the potential of LF as a functional food ingredient to prevent bacterial infection. View Full-Text
Keywords: lactoferrin; glycosylation; surface plasmon resonance; bacterial binding; lactation lactoferrin; glycosylation; surface plasmon resonance; bacterial binding; lactation
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

O’Riordan, N.; Kilcoyne, M.; Joshi, L.; Hickey, R.M. Exploitation of SPR to Investigate the Importance of Glycan Chains in the Interaction between Lactoferrin and Bacteria. Sensors 2017, 17, 1515.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Sensors EISSN 1424-8220 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top